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Reverse turns in peptides and proteins

J A Smith, L G Pease

    CRC Critical Reviews in Biochemistry
    |January 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

    This review highlights the prevalence of reverse turns in proteins and peptides. It critically examines experimental and theoretical evidence, linking these structures to biological function and recognition.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Peptide Chemistry

    Background:

    • Reverse turns are common structural motifs in proteins and peptides.
    • Understanding their formation and function is crucial for molecular biology.

    Purpose of the Study:

    • To critically review experimental and theoretical evidence for reverse turn structures.
    • To evaluate the relationship between reverse turn structure and biological function.

    Main Methods:

    • Experimental physical methods: NMR spectroscopy (1H, 13C), spin-lattice relaxation time, circular dichroism, IR spectroscopy, X-ray crystallography.
    • Theoretical methods: Energy calculations using empirical energy functions, correlative methods based on amino acid frequency algorithms.

    Main Results:

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    • Overwhelming evidence supports the frequent occurrence of reverse turns in various biomolecules.
    • Emphasis on theoretical studies with complementary physical validation.
    • Demonstration of structure-function relationships and biological recognition involving reverse turns.

    Conclusions:

    • Reverse turns are integral to protein and peptide structure.
    • Integrated experimental and theoretical approaches provide robust insights.
    • Reverse turns play significant roles in biological recognition and function.